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    Probing the Molecular Mechanisms of Quartz-Binding Peptides
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    † Department of Materials Science and Engineering, University of Washington, Seattle, Washington
    ‡ Department of Microbiology, University of Washington, Seattle, Washington
    § Department of Chemistry, University of Warwick, Coventry, CV4 7AL, U.K.
    ⊥ Laboratory for Chemical Physics, New York University, New York, New York, 10010
    Centre for Scientific Computing, University of Warwick, Coventry, CV4 7AL, U.K.
    # Molecular Biology and Genetics, Istanbul Technical University, Maslak, Istanbul, 80626, Turkey
    *To whom correspondence should be addressed. E-mail: [email protected]. Tel.: +1 206 543 0724. Fax: +1 206 543 6381. Address: Materials Science and Engineering, University of Washington, 327 Roberts Hall, Box 352120, Seattle, WA, 98195.
    ∇Denotes joint first authors.
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    Langmuir

    Cite this: Langmuir 2010, 26, 13, 11003–11009
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    https://doi.org/10.1021/la100049s
    Published May 25, 2010
    Copyright © 2010 American Chemical Society
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    Abstract

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    Understanding the mechanisms of biomineralization and the realization of biology-inspired inorganic materials formation largely depends on our ability to manipulate peptide/solid interfacial interactions. Material interfaces and biointerfaces are critical sites for bioinorganic synthesis, surface diffusion, and molecular recognition. Recently adapted biocombinatorial techniques permit the isolation of peptides recognizing inorganic solids that are used as molecular building blocks, for example, as synthesizers, linkers, and assemblers. Despite their ubiquitous utility in nanotechnology, biotechnology, and medicine, the fundamental mechanisms of molecular recognition of engineered peptides binding to inorganic surfaces remain largely unknown. To explore propensity rules connecting sequence, structure, and function that play key roles in peptide/solid interactions, we combine two different approaches: a statistical analysis that searches for highly enriched motifs among de novo designed peptides, and, atomistic simulations of three experimentally validated peptides. The two strong and one weak quartz-binding peptides were chosen for the simulations at the quartz (100) surface under aqueous conditions. Solution-based peptide structures were analyzed by circular dichroism measurements. Small and hydrophobic residues, such as Pro, play a key role at the interface by making close contact with the solid and hindering formation of intrapeptide hydrogen bonds. The high binding affinity of a peptide may be driven by a combination of favorable enthalpic and entropic effects, that is, a strong binder may possess a large number of possible binding configurations, many of which having relatively high binding energies. The results signify the role of the local molecular environment among the critical residues that participate in solid binding. The work herein describes molecular conformations inherent in material-specific peptides and provides fundamental insight into the atomistic understanding of peptide/solid interfaces.

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    Methodological details on the REMD and peptide−surface simulations and cluster and flexibility analyses; figures showing SPR and Q-dot immobilization assays and peptide/surface interaction energies; tables containing contact residues and their time averaged distances to the surface. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cite this: Langmuir 2010, 26, 13, 11003–11009
    Click to copy citationCitation copied!
    https://doi.org/10.1021/la100049s
    Published May 25, 2010
    Copyright © 2010 American Chemical Society
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